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Literature summary extracted from

  • Bee, G.; Waller, J.P.
    Valyl-tRNA synthetase from rabbit liver. II. The enzyme derived from the high-Mr complex displays hydrophobic as well as polyanion-binding properties (1989), J. Biol. Chem., 264, 21138-21143.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.1.1.9 125000
-
 1 * 125000, SDS-PAGE Saccharomyces cerevisiae
6.1.1.9 135000
-
 glycerol density gradient centrifugation Oryctolagus cuniculus
6.1.1.9 140000
-
 1 * 140000, SDS-PAGE Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.9 Oryctolagus cuniculus
-
-
-
6.1.1.9 Saccharomyces cerevisiae
-
-
-
6.1.1.9 Saccharomyces cerevisiae D273
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.1.1.9 liver
-
 Oryctolagus cuniculus
-

Storage Stability

EC Number Storage Stability Organism
6.1.1.9 -20°C, 50% glycerol, 0.1% detergent, stable for several months Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.9 ATP + L-valine + tRNAVal
-
 Saccharomyces cerevisiae AMP + diphosphate + L-valyl-tRNAVal
-
 ?
6.1.1.9 ATP + L-valine + tRNAVal
-
 Oryctolagus cuniculus AMP + diphosphate + L-valyl-tRNAVal
-
 ?
6.1.1.9 ATP + L-valine + tRNAVal
-
 Saccharomyces cerevisiae D273 AMP + diphosphate + L-valyl-tRNAVal
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.9 ?
-
 Oryctolagus cuniculus
6.1.1.9 monomer 1 * 140000, SDS-PAGE Oryctolagus cuniculus
6.1.1.9 monomer 1 * 125000, SDS-PAGE Saccharomyces cerevisiae